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1fvg

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Revision as of 13:12, 20 November 2007 by OCA (Talk | contribs)
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1fvg, resolution 1.6Å

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CRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASE

Overview

Peptide methionine sulfoxide reductase (MsrA) reverses oxidative damage to, both free methionine and methionine within proteins. As such, it helps, protect the host organism against stochastic damage that can contribute to, cell death. The structure of bovine MsrA has been determined in two, different modifications, both of which provide different insights into the, biology of the protein. There are three cysteine residues located in the, vicinity of the active site. Conformational changes in a glycine-rich, C-terminal tail appear to allow all three thiols to come together and to, participate in catalysis. The structures support a unique, thiol-disulfide, exchange mechanism that relies upon an essential cysteine as a nucleophile, and additional conserved residues that interact with the oxygen atom of, the sulfoxide moiety.

About this Structure

1FVG is a Single protein structure of sequence from Bos taurus with DTT as ligand. Active as Peptide-methionine-(S)-S-oxide reductase, with EC number 1.8.4.11 Full crystallographic information is available from OCA.

Reference

Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme., Lowther WT, Brot N, Weissbach H, Matthews BW, Biochemistry. 2000 Nov 7;39(44):13307-12. PMID:11063566

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